Search results for "HEK 293"

showing 10 items of 73 documents

Ataluren for the Treatment of Usher Syndrome 2A Caused by Nonsense Mutations

2019

The identification of genetic defects that underlie inherited retinal diseases (IRDs) paves the way for the development of therapeutic strategies. Nonsense mutations caused approximately 12% of all IRD cases, resulting in a premature termination codon (PTC). Therefore, an approach that targets nonsense mutations could be a promising pharmacogenetic strategy for the treatment of IRDs. Small molecules (translational read-through inducing drugs

0301 basic medicinepatient-derived fibroblastsUsher syndromechemistry.chemical_compound0302 clinical medicineMedicineTRIDSpectroscopyCells CulturedExtracellular Matrix ProteinsOxadiazolesGeneral MedicinePhenotypeImmunohistochemistryComputer Science ApplicationsRetinitis pigmentosaCodon Nonsenseocular therapyUsher syndromeUsher SyndromesNonsense mutationModels BiologicalCatalysisArticleInorganic Chemistry03 medical and health sciencesStructure-Activity RelationshipAtalurenCiliogenesisparasitic diseasesRetinitis pigmentosaHumansGenetic Predisposition to DiseasePhysical and Theoretical ChemistryMolecular BiologyGenetranslational read-throughbusiness.industryOrganic ChemistryHEK 293 cellsFibroblastsmedicine.diseaseAtaluren030104 developmental biologyHEK293 CellschemistryProtein BiosynthesisMutationCancer researchbusiness030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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Autoradiographic imaging of altered synaptic αβγ2 and extrasynaptic αβ GABAA receptors in a genetic mouse model of anxiety

2004

Abstract To image the possible alterations in brain regional GABAA receptor subtype properties in a genetic animal model of human anxiety, mice heterozygous for the deletion of GABAA receptor γ2 subunit (γ2+/−) were studied using ligand autoradiographic assays on brain cryostat sections. The [ 35 S ]TBPS binding assay was designed to reveal impaired GABA and channel site coupling shown to be more prominent in recombinant α1/6β3 than in α1/2β3γ2 or β2 subunit-containing GABAA receptors expressed in HEK 293 cells. Increased GABA-insensitive [ 35 S ]TBPS binding in the γ2+/− mouse brains was evident in the cerebral cortex and in subcortical regions, the alterations being regionally similar to …

0303 health sciencesmedicine.medical_specialtyBenzodiazepineGABAA receptormedicine.drug_classLigand binding assayHEK 293 cellsCell BiologyBiologyGABAA-rho receptorCell biology03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinemedicine.anatomical_structureEndocrinologyCerebral cortexInternal medicinemedicineBinding siteReceptor030217 neurology & neurosurgery030304 developmental biologyNeurochemistry International
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Shedding of the amyloid precursor protein-like protein APLP2 by disintegrin-metalloproteinases

2005

Cleavage of the amyloid precursor protein (APP) within the amyloid-beta (Aβ) sequence by the α-secretase prevents the formation of toxic Aβ peptides. It has been shown that the disintegrin-metalloproteinases ADAM10 and TACE (ADAM17) act as α-secretases and stimulate the generation of a soluble neuroprotective fragment of APP, APPsα. Here we demonstrate that the related APP-like protein 2 (APLP2), which has been shown to be essential for development and survival of mice, is also a substrate for both proteinases. Overexpression of either ADAM10 or TACE in HEK293 cells increased the release of neurotrophic soluble APLP2 severalfold. The strongest inhibition of APLP2 shedding in neuroblastoma c…

ADAM10HEK 293 cellsRetinoic acidP3 peptideCell BiologyBiologyBiochemistryMolecular biologychemistry.chemical_compoundchemistryDownregulation and upregulationbiology.proteinAmyloid precursor proteinMolecular BiologyAPLP2Amyloid precursor protein secretaseFEBS Journal
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Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

1999

Amyloid β peptide (Aβ), the principal proteinaceous component of amyloid plaques in brains of Alzheimer’s disease patients, is derived by proteolytic cleavage of the amyloid precursor protein (APP). Proteolytic cleavage of APP by a putative α-secretase within the Aβ sequence precludes the formation of the amyloidogenic peptides and leads to the release of soluble APPsα into the medium. By overexpression ofa disintegrinandmetalloprotease (ADAM), classified as ADAM 10, in HEK 293 cells, basal and protein kinase C-stimulated α-secretase activity was increased severalfold. The proteolytically activated form of ADAM 10 was localized by cell surface biotinylation in the plasma membrane, but the m…

ADAM10Molecular Sequence DataBiologyKidneyTransfectionCell LineSubstrate SpecificityADAM10 ProteinAmyloid beta-Protein PrecursorEndopeptidasesAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansPoint MutationADAM17 ProteinAmino Acid SequenceCloning MolecularProtein kinase AProtein Kinase CSecretory pathwayBinding SitesMultidisciplinaryHEK 293 cellsP3 peptideMembrane ProteinsMetalloendopeptidasesBiological SciencesPeptide FragmentsRecombinant Proteinscarbohydrates (lipids)ADAM ProteinsKineticsZincAlpha secretaseBiochemistryMutagenesis Site-Directedbiology.proteinCattleAmyloid Precursor Protein SecretasesProceedings of the National Academy of Sciences
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Elevated levels of Bcl-3 inhibits Treg development and function resulting in spontaneous colitis

2017

Bcl-3 is an atypical NF-κB family member that regulates NF-κB-dependent gene expression in effector T cells, but a cell-intrinsic function in regulatory T (Treg) cells and colitis is not clear. Here we show that Bcl-3 expression levels in colonic T cells correlate with disease manifestation in patients with inflammatory bowel disease. Mice with T-cell-specific overexpression of Bcl-3 develop severe colitis that can be attributed to defective Treg cell development and function, leading to the infiltration of immune cells such as pro-inflammatory γδT cells, but not αβ T cells. In Treg cells, Bcl-3 associates directly with NF-κB p50 to inhibit DNA binding of p50/p50 and p50/p65 NF-κB dimers, t…

AdultMale0301 basic medicineP50ScienceGeneral Physics and AstronomyBiologyT-Lymphocytes RegulatoryInflammatory bowel diseaseArticleGeneral Biochemistry Genetics and Molecular BiologyYoung Adult03 medical and health sciences0302 clinical medicineImmune systemB-Cell Lymphoma 3 ProteinProto-Oncogene ProteinsGene expressionmedicineAnimalsHumansColitisMice KnockoutRegulation of gene expressionMultidisciplinaryEffectorHEK 293 cellsQNF-kappa BTranscription Factor RelANF-kappa B p50 SubunitGeneral ChemistryMiddle AgedColitismedicine.diseaseMice Inbred C57BLHEK293 Cells030104 developmental biologyGene Expression Regulation030220 oncology & carcinogenesisImmunologyFemaleProtein BindingTranscription FactorsNature Communications
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Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family

2011

Fibroblast growth factor receptor 1 (FGFR1) is known to be activated by homodimerization in the presence of both the FGF agonist ligand and heparan sulfate glycosaminoglycan. FGFR1 homodimers in turn trigger a variety of downstream signaling cascades via autophosphorylation of tyrosine residues in the cytoplasmic domain of FGFR1. By means of Bioluminescence Energy Resonance Transfer (BRET) as a sign of FGFR1 homodimerization, we evaluated in HEK293T cells the effects of all known FGF agonist ligands on homodimer formation. A significant correlation between BRET(2) signaling and ERK1/2 phosphorylation was observed, leading to a further characterization of the binding and signaling properties…

AgonistMAPK/ERK pathwaymedicine.drug_classBiophysicsSettore BIO/11 - Biologia MolecolareBiologyLigandsFibroblast growth factorSettore BIO/09 - FisiologiaBiochemistrychemistry.chemical_compoundFluorescence Resonance Energy TransfermedicineHumansReceptor Fibroblast Growth Factor Type 1Molecular BiologyMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Fibroblast growth factor receptor 1HEK 293 cellsAutophosphorylationCell BiologyHeparan sulfateFibroblast growth factors FGFR1 Homodimerization BRET MAPKCell biologyFibroblast Growth Factorsstomatognathic diseasesHEK293 CellschemistrySettore BIO/14 - FarmacologiaPhosphorylationHeparitin SulfateProtein MultimerizationBiochemical and Biophysical Research Communications
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Cellular stress induces cap-independent alpha-enolase/MBP-1 translation.

2015

AbstractMyc promoter-binding protein-1 (MBP-1) is a shorter protein variant of the glycolytic enzyme alpha-enolase. Although several lines of evidence indicate that MBP-1 acts as a tumor suppressor, the cellular mechanisms and signaling pathways underlying MBP-1 expression still remain largely elusive. To dissect these pathways, we used the SkBr3 breast cancer cell line and non-tumorigenic HEK293T cells ectopically overexpressing alpha-enolase/MBP-1. Here, we demonstrate that induced cell stresses promote MBP-1 expression through the AKT/PERK/eIF2α signaling axis. Our results contribute to shedding light on the molecular mechanisms underlying MBP-1 expression in non-tumorigenic and cancer c…

Alpha-enolaseCellEukaryotic Initiation Factor-2Alternative translationBiochemistryeIF-2 KinaseBreast cancerHEK293 CellStructural BiologyProtein IsoformsbiologyMedicine (all)Translation (biology)Recombinant ProteinEndoplasmic Reticulum StressRecombinant ProteinsNeoplasm ProteinsDNA-Binding ProteinsGene Expression Regulation Neoplasticmedicine.anatomical_structureFemaleSignal transductionMyc promoter-binding protein-1Breast NeoplasmHumanSignal TransductionCell SurvivalDNA-Binding ProteinRecombinant Fusion ProteinsBiophysicsBreast NeoplasmsNeoplasm ProteinGeneticCell Line TumorEndoplasmic reticulum streGeneticsmedicineBiomarkers TumorHumansGene SilencingMolecular BiologyProtein kinase BTumor Suppressor ProteinTumor Suppressor ProteinsHEK 293 cellsProtein IsoformCell BiologySettore BIO/18 - GeneticaHEK293 CellsBiophysicGene Expression RegulationPhosphopyruvate HydrataseCancer cellbiology.proteinUnfolded protein responseCancer researchProto-Oncogene Proteins c-aktRecombinant Fusion ProteinFEBS letters
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The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3- exchanger DRA in rabbit small intestinal mucosa.

2005

DRA (down regulated in adenoma) is an intestinal anion exchanger, acting in parallel with NHE3 to facilitate ileal and colonic NaCl absorption. Furthermore it is involved in small intestinal bicarbonate secretion. Because DRA has a PDZ interaction motif, which may influence its properties, we searched for DRA-interacting PDZ adapter proteins in the small intestine. Using an overlay assay with the recombinant DRA C-terminus as a ligand, a 70 kDa protein was labeled, which was restricted to the brush border membrane in rabbit duodenal and ileal mucosa and was not detected in the colon. Destruction of the C-terminal PDZ interaction motif abolished this band, suggesting a specific protein-prote…

Brush borderColonPDZ domainAmino Acid MotifsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorIleumBiologyBiochemistryAntiportersCell LineIntestine SmallmedicineAnimalsHumansSecretionAmino Acid SequenceChloride-Bicarbonate AntiportersRNA MessengerIntestinal MucosaMessenger RNAHEK 293 cellsSignal transducing adaptor proteinMembrane ProteinsMolecular biologySmall intestinePeptide Fragmentsmedicine.anatomical_structureSulfate TransportersRabbitsCarrier ProteinsBiochemistry
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T-cell receptor transfer into human T cells with ecotropic retroviral vectors

2014

Adoptive T-cell transfer for cancer immunotherapy requires genetic modification of T cells with recombinant T-cell receptors (TCRs). Amphotropic retroviral vectors (RVs) used for TCR transduction for this purpose are considered safe in principle. Despite this, TCR-coding and packaging vectors could theoretically recombine to produce replication competent vectors (RCVs), and transduced T-cell preparations must be proven free of RCV. To eliminate the need for RCV testing, we transduced human T cells with ecotropic RVs so potential RCV would be non-infectious for human cells. We show that transfection of synthetic messenger RNA encoding murine cationic amino-acid transporter 1 (mCAT-1), the re…

CD4-Positive T-LymphocytesAdoptive cell transfermedicine.medical_treatmentGenetic enhancementGenetic VectorsReceptors Antigen T-CellCD8-Positive T-LymphocytesBiologyImmunotherapy AdoptiveJurkat cellsVesicular stomatitis Indiana virusCell LineJurkat CellsMiceTransduction (genetics)Viral Envelope ProteinsCancer immunotherapyTransduction GeneticGeneticsmedicineAnimalsHumansRNA MessengerMolecular BiologyCationic Amino Acid Transporter 1Membrane GlycoproteinsHEK 293 cellsT-cell receptorTransfectionAdoptive TransferVirologyElectroporationHEK293 CellsRetroviridaeLeukemia Virus Gibbon ApeMolecular MedicinePlasmidsGene Therapy
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The human Lgl polarity gene, Hugl-2, induces MET and suppresses Snail tumorigenesis

2012

Lethal giant larvae proteins have key roles in regulating polarity in a variety of cell types and function as tumour suppressors. A transcriptional programme initiated by aberrant Snail expression transforms epithelial cells to potentially aggressive cancer cells. Although progress in defining the molecular determinants of this programme has been made, we have little knowledge as to how the Snail-induced phenotype can be suppressed. In our studies we identified the human lethal giant larvae homologue 2, Hugl-2, (Llgl2/Lgl2) polarity gene as downregulated by Snail. Snail binds E-boxes in the Hugl-2 promoter and represses Hugl-2 expression, whereas removal of the E-boxes releases Hugl-2 from …

Cancer ResearchCell typeMice SCIDSnailmedicine.disease_causeMiceMice Inbred NODbiology.animalChlorocebus aethiopsparasitic diseasesCell polarityGeneticsmedicineAnimalsHumansGenes Tumor SuppressorNeoplasm MetastasisMolecular BiologyTranscription factorCells CulturedRegulation of gene expressionbiologyfungiHEK 293 cellsCell PolarityHep G2 CellsAnatomyProto-Oncogene Proteins c-metXenograft Model Antitumor AssaysPhenotypeUp-RegulationCell biologyGene Expression Regulation NeoplasticCytoskeletal ProteinsCell Transformation NeoplasticHEK293 CellsCOS CellsSnail Family Transcription FactorsCarcinogenesisProtein BindingTranscription FactorsOncogene
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